Fischer-Tropsch (F-T) process is an important synthesis route to acquire clean liquid fuels through modern coal chemical industry, which converts syngas (CO and H2) into hydrocarbon, and also generates oxygenates discharged as the F-T waste-water. These oxygen-containing compounds in F-T waste-water have the similar molecular weight and some are even isomers of each other. Hence, it is necessary to develop rapid and efficient analysis tools to obtain identification and quantitative information of the F-T waste-water. The pure shift NMR techniques provided only chemical shift information in one-dimension 1H NMR spectra, without homonuclear JH-H coupling. In this work, we tested and compared three pure shift NMR techniques (including Zangger-Sterk, PSYCHE and TSE-PSYCHE methods) in the analysis of two F-T waste-water model mixtures, genuine waste-water and two alcohol isomer mixtures. The results show that JH-H coupling multiplicities are collapsed into singlets corresponding to individual chemically distinct protons of the compound. For some severely overlapped signals in the pure shift NMR spectra, the chemical shift selective filters with TOCSY (CSSF-TOCSY) experiments were conducted to assist the signal assignment. Thus, pure shift NMR approaches can identify most signals of components, and CSSF-TOCSY can extract the signal of a specific compound. The combination of these two NMR techniques offers a powerful tool to analyze the F-T waste-water or other complex mixtures including isomer mixtures. The chemical interaction between antifreeze proteins (AFPs) and ice crystals is evaluated via electrophoresis of AFP-anchored microparticles in fluidic channels formed in frozen aqueous sucrose. Straight fluidic channels are created in a flat glass chamber connecting two Ag/AgCl electrodes. This configuration allows us to estimate an electric field strength exerted on probe particles migrating along the channel. When the channel width is comparable to the particle size, the particle is immobile because of the resistance force induced by the interaction with the ice wall. However, when the overall electrophoretic force surpasses the resistance force, the microsphere starts to migrate. From the threshold electric field strengths determined for unmodified and AFP-modified particles, the resistance forces for the chemical interaction between AFPs and ice wall are estimated. DNA aptamers were selected for their ability to bind specifically and quickly to crystalline hydroxyapatite (Ca10(PO4)6(OH)2; HAP), the primary mineral component of enamel and bone. Aptamers were found to have an enhanced percent of G-nucleotides and a propensity for forming a G-quadruplex secondary structure. One aptamer was studied in comparison to control sequences and was found to bind with high affinity and at high loading capacity, with enhanced binding kinetics, and with specificity for crystalline HAP material over amorphous calcium phosphate (ACP) and β-tricalcium phosphate (TCP). The fluorescently-functionalized aptamer was demonstrated to specifically label HAP in a surface binding experiment and suggests the usefulness of this selected aptamer in biomedical or biotechnology fields where the labeling of specific calcium phosphate materials is required. The analysis of siliceous matrix samples may adopt a two-step pretreatment, which includes melting with ammonium hydrogen fluoride and redissolving with nitric acid. However, the residual of substrate silicon unfavorable to the determination of trace elements in the samples due to serious matrix effects. Here, a new digestion method using simultaneously both ammonium bifluoride and nitric acid under normal pressure was developed for high-purity quartz sand sample. The digestion pretreatment is a two step process melting/dissolving with both ammonium bifluoride and nitric acid at 200&nbsp;°C for 2&nbsp;h, and evaporating the solution at 250&nbsp;°C to dryness. As confirmed by XRD analysis, silicates in the sample were converted to (NH4)3SiF6NO3 in the melting/dissolving step. TGA analysis shows that the generated (NH4)3SiF6NO3 could be decomposed and evaporated completely at 250&nbsp;°C, which ensured a complete removal of silicon by the followed evaporation of the solution at 250&nbsp;°C. As a result, the followed ICP-OES and ICP-MS analysis needed a solution dilution of only 100 times for the determination of Ca, Mg, Al, Rb, Ba, REE and other trace elements. The new method was applied to the analysis of three certified reference materials, and the results were well consistent with the standard value with RSD% values between 0.62% and 9.73%. Therefore, this method can be applied to the analysis of trace elements in high purity silica-based samples, with the advantages of time-saving, small dilution factor (only 100 times) and low detection limit. Resolution is an essential challenge in NMR spectroscopy. Narrow chemical shift range and extensive signal splittings due to scalar couplings often give rise to spectral congestion and even overlap in NMR spectra. Magnetic field strength is directly responsible for spectral resolution as higher magnetic field strength offers better signal dispersion. However, the process of further increasing magnetic field strength of NMR instruments is slow and expensive. Methodology aimed at resolution issue has long been developing. Here, we present a chemical shift upscaling method, in which chemical shifts are upscaled by a given factor while scalar couplings are unchanged. As a result, signal dispersion and hence the resolution are improved. Therefore, it is possible to separate multiplets which originally overlap with each other and to extract their integrals for quantitative analysis. Improved signal dispersion and the preservation of scalar couplings also facilitate multiplet analysis and signal assignment. https://www.selleckchem.com/products/crt-0105446.html Chemical shift upscaling offers a method for enhancing resolution limited by magnetic field strength. Understanding the binding affinities and kinetics of protein-ligand interactions using a label-free method is crucial for identifying therapeutic candidates in clinical diagnostics and drug development. In this work, the IGZO-TFT (thin-film transistor) biosensor integrated with a tailored microfluidic chip was developed to explore binding kinetics of protein-ligand biochemical interactions in the real-time manner. The IGZO-TFT sensor extracts the binding characteristics through sensing biomolecules by their electrical charges. Using lysozyme and tri-N-acetyl-D-glucosamine (NAG3) as an example, we established a procedure to obtain the parameters, such as the dissociation constant, Kd, and association rate constant, ka, that are critical to biochemical reactions. The correlation between the lysozyme concentration and TFT drain current signal was first constructed. Next, solutions of lysozyme and NAG3 of different mixing ratios were prepared. They were pre-mixed for various periods of reaction time before applying to the TFT sensor to extract signals of lysozyme molecules and the concentration remaining.